DePaoli-Roach A A, Lee F T
FEBS Lett. 1985 Apr 22;183(2):423-9. doi: 10.1016/0014-5793(85)80824-3.
Phosphoprotein phosphatase inhibitor-2 (i-2) was rapidly isolated from mouse diaphragm extracts by the use of specific antibodies. The i-2 so obtained was associated with ATP-Mg and FA/GSK-3 dependent phosphatase activity, supporting the idea that i-2 is in fact a component of this form of phosphatase. Inhibitor-2 isolated from diaphragms incubated with [32P]phosphate contained both phosphoserine (approximately 90%) and phosphothreonine (approximately 10%). Therefore, i-2 is multiply phosphorylated in mouse diaphragm and the potential exists for control of the ATP-Mg-dependent phosphatase via multiple phosphorylation sites in vivo.
通过使用特异性抗体，从小鼠膈肌提取物中快速分离出磷蛋白磷酸酶抑制剂-2（i-2）。如此获得的i-2与ATP-Mg以及FA/GSK-3依赖性磷酸酶活性相关，支持了i-2实际上是这种形式磷酸酶的一个组分的观点。从用[32P]磷酸盐孵育的膈肌中分离出的抑制剂-2同时含有磷酸丝氨酸（约90%）和磷酸苏氨酸（约10%）。因此，i-2在小鼠膈肌中被多重磷酸化，并且在体内通过多个磷酸化位点控制ATP-Mg依赖性磷酸酶的可能性存在。
